Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Histone deacetylase 1 (HD1) (EC 3.5.1.98)

 HDAC1_HUMAN             Reviewed;         482 AA.
Q13547; Q92534;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 1.
22-NOV-2017, entry version 210.
RecName: Full=Histone deacetylase 1;
Short=HD1;
EC=3.5.1.98;
Name=HDAC1; Synonyms=RPD3L1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=T-cell;
PubMed=8602529; DOI=10.1126/science.272.5260.408;
Taunton J., Hassig C.A., Schreiber S.L.;
"A mammalian histone deacetylase related to the yeast transcriptional
regulator Rpd3p.";
Science 272:408-411(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Fetal lung;
PubMed=8646880;
Furukawa Y., Kawakami T., Sudo K., Inazawa J., Matsumine A.,
Akiyama T., Nakamura Y.;
"Isolation and mapping of a human gene (RPD3L1) that is homologous to
RPD3, a transcription factor in Saccharomyces cerevisiae.";
Cytogenet. Cell Genet. 73:130-133(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
INTERACTION WITH HDAC9.
PubMed=10487760; DOI=10.1093/emboj/18.18.5085;
Sparrow D.B., Miska E.A., Langley E., Reynaud-Deonauth S., Kotecha S.,
Towers N., Spohr G., Kouzarides T., Mohun T.J.;
"MEF-2 function is modified by a novel co-repressor, MITR.";
EMBO J. 18:5085-5098(1999).
[5]
INTERACTION WITH BCOR.
PubMed=10898795;
Huynh K.D., Fischle W., Verdin E., Bardwell V.J.;
"BCoR, a novel corepressor involved in BCL-6 repression.";
Genes Dev. 14:1810-1823(2000).
[6]
INTERACTION WITH THE 9-1-1 COMPLEX AND HUS1, AND SUBCELLULAR LOCATION.
PubMed=10846170; DOI=10.1074/jbc.M000168200;
Cai R.L., Yan-Neale Y., Cueto M.A., Xu H., Cohen D.;
"HDAC1, a histone deacetylase, forms a complex with Hus1 and Rad9, two
G2/M checkpoint Rad proteins.";
J. Biol. Chem. 275:27909-27916(2000).
[7]
INTERACTION WITH NRIP1.
PubMed=11006275; DOI=10.1074/jbc.M004821200;
Wei L.-N., Hu X., Chandra D., Seto E., Farooqui M.;
"Receptor-interacting protein 140 directly recruits histone
deacetylases for gene silencing.";
J. Biol. Chem. 275:40782-40787(2000).
[8]
INTERACTION WITH DAXX.
PubMed=10669754; DOI=10.1128/MCB.20.5.1784-1796.2000;
Li H., Leo C., Zhu J., Wu X., O'Neil J., Park E.-J., Chen J.D.;
"Sequestration and inhibition of Daxx-mediated transcriptional
repression by PML.";
Mol. Cell. Biol. 20:1784-1796(2000).
[9]
INTERACTION WITH HDAC9.
PubMed=10655483; DOI=10.1073/pnas.97.3.1056;
Zhou X., Richon V.M., Rifkind R.A., Marks P.A.;
"Identification of a transcriptional repressor related to the
noncatalytic domain of histone deacetylases 4 and 5.";
Proc. Natl. Acad. Sci. U.S.A. 97:1056-1061(2000).
[10]
PHOSPHORYLATION AT SER-421 AND SER-423, MUTAGENESIS OF SER-421 AND
SER-423, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=11602581; DOI=10.1074/jbc.M105590200;
Pflum M.K.H., Tong J.K., Lane W.S., Schreiber S.L.;
"Histone deacetylase 1 phosphorylation promotes enzymatic activity and
complex formation.";
J. Biol. Chem. 276:47733-47741(2001).
[11]
INTERACTION WITH MINT.
PubMed=11331609; DOI=10.1101/gad.871201;
Shi Y., Downes M., Xie W., Kao H.-Y., Ordentlich P., Tsai C.-C.,
Hon M., Evans R.M.;
"Sharp, an inducible cofactor that integrates nuclear receptor
repression and activation.";
Genes Dev. 15:1140-1151(2001).
[12]
INTERACTION WITH MBD2 AND MBD3.
PubMed=11102443; DOI=10.1074/jbc.M007372200;
Humphrey G.W., Wang Y., Russanova V.R., Hirai T., Qin J., Nakatani Y.,
Howard B.H.;
"Stable histone deacetylase complexes distinguished by the presence of
SANT domain proteins CoREST/kiaa0071 and Mta-L1.";
J. Biol. Chem. 276:6817-6824(2001).
[13]
INTERACTION WITH TGIF2.
PubMed=11427533; DOI=10.1074/jbc.M103377200;
Melhuish T.A., Gallo C.M., Wotton D.;
"TGIF2 interacts with histone deacetylase 1 and represses
transcription.";
J. Biol. Chem. 276:32109-32114(2001).
[14]
INTERACTION WITH CBFA2T3.
PubMed=11533236; DOI=10.1128/MCB.21.19.6470-6483.2001;
Amann J.M., Nip J., Strom D.K., Lutterbach B., Harada H., Lenny N.,
Downing J.R., Meyers S., Hiebert S.W.;
"ETO, a target of t(8;21) in acute leukemia, makes distinct contacts
with multiple histone deacetylases and binds mSin3A through its
oligomerization domain.";
Mol. Cell. Biol. 21:6470-6483(2001).
[15]
SUMOYLATION.
PubMed=12032081; DOI=10.1093/emboj/21.11.2682;
Kirsh O., Seeler J.-S., Pichler A., Gast A., Mueller S., Miska E.,
Mathieu M., Harel-Bellan A., Kouzarides T., Melchior F., Dejean A.;
"The SUMO E3 ligase RanBP2 promotes modification of the HDAC4
deacetylase.";
EMBO J. 21:2682-2691(2002).
[16]
SUMOYLATION AT LYS-444 AND LYS-476.
PubMed=11960997; DOI=10.1074/jbc.M203690200;
David G., Neptune M.A., DePinho R.A.;
"SUMO-1 modification of histone deacetylase 1 (HDAC1) modulates its
biological activities.";
J. Biol. Chem. 277:23658-23663(2002).
[17]
INTERACTION WITH APEX1.
PubMed=14633989; DOI=10.1093/emboj/cdg595;
Bhakat K.K., Izumi T., Yang S.H., Hazra T.K., Mitra S.;
"Role of acetylated human AP-endonuclease (APE1/Ref-1) in regulation
of the parathyroid hormone gene.";
EMBO J. 22:6299-6309(2003).
[18]
INTERACTION WITH HCFC1.
PubMed=12670868; DOI=10.1101/gad.252103;
Wysocka J., Myers M.P., Laherty C.D., Eisenman R.N., Herr W.;
"Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4
methyltransferase are tethered together selectively by the cell-
proliferation factor HCF-1.";
Genes Dev. 17:896-911(2003).
[19]
IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE BHC
COMPLEX WITH GSE1; GTF2I; HDAC2; HMG20B; KDM1A; PHF21A; RCOR1; ZMYM2;
ZMYM3 AND ZNF217.
PubMed=12493763; DOI=10.1074/jbc.M208992200;
Hakimi M.-A., Dong Y., Lane W.S., Speicher D.W., Shiekhattar R.;
"A candidate X-linked mental retardation gene is a component of a new
family of histone deacetylase-containing complexes.";
J. Biol. Chem. 278:7234-7239(2003).
[20]
INTERACTION WITH SP3, AND FUNCTION.
PubMed=12837748; DOI=10.1074/jbc.M305961200;
Ammanamanchi S., Freeman J.W., Brattain M.G.;
"Acetylated SP3 is a transcriptional activator.";
J. Biol. Chem. 278:35775-35780(2003).
[21]
INTERACTION WITH MIER1.
PubMed=12482978; DOI=10.1128/MCB.23.1.250-258.2003;
Ding Z., Gillespie L.L., Paterno G.D.;
"Human MI-ER1 alpha and beta function as transcriptional repressors by
recruitment of histone deacetylase 1 to their conserved ELM2 domain.";
Mol. Cell. Biol. 23:250-258(2003).
[22]
IDENTIFICATION IN A MSIN3A COREPRESSOR COMPLEX WITH SIN3A; SAP130;
SUDS3; ARID4B; HDAC1 AND HDAC2.
PubMed=12724404; DOI=10.1128/MCB.23.10.3456-3467.2003;
Fleischer T.C., Yun U.J., Ayer D.E.;
"Identification and characterization of three new components of the
mSin3A corepressor complex.";
Mol. Cell. Biol. 23:3456-3467(2003).
[23]
INTERACTION WITH E4F1.
PubMed=12730668; DOI=10.1038/sj.onc.1206379;
Colombo R., Draetta G.F., Chiocca S.;
"Modulation of p120E4F transcriptional activity by the Gam1 adenoviral
early protein.";
Oncogene 22:2541-2547(2003).
[24]
INTERACTION WITH BRMS1L.
PubMed=15451426; DOI=10.1016/j.bbrc.2004.08.227;
Nikolaev A.Y., Papanikolaou N.A., Li M., Qin J., Gu W.;
"Identification of a novel BRMS1-homologue protein p40 as a component
of the mSin3A/p33(ING1b)/HDAC1 deacetylase complex.";
Biochem. Biophys. Res. Commun. 323:1216-1222(2004).
[25]
INTERACTION WITH BCL6, AND IDENTIFICATION IN THE NURD COMPLEX.
PubMed=15454082; DOI=10.1016/j.cell.2004.09.014;
Fujita N., Jaye D.L., Geigerman C., Akyildiz A., Mooney M.R.,
Boss J.M., Wade P.A.;
"MTA3 and the Mi-2/NuRD complex regulate cell fate during B lymphocyte
differentiation.";
Cell 119:75-86(2004).
[26]
INTERACTION WITH NFE4.
PubMed=15273251; DOI=10.1074/jbc.M405129200;
Zhao Q., Cumming H., Cerruti L., Cunningham J.M., Jane S.M.;
"Site-specific acetylation of the fetal globin activator NF-E4
prevents its ubiquitination and regulates its interaction with the
histone deacetylase, HDAC1.";
J. Biol. Chem. 279:41477-41486(2004).
[27]
DESUMOYLATION BY SENP1.
PubMed=15199155; DOI=10.1128/MCB.24.13.6021-6028.2004;
Cheng J., Wang D., Wang Z., Yeh E.T.H.;
"SENP1 enhances androgen receptor-dependent transcription through
desumoylation of histone deacetylase 1.";
Mol. Cell. Biol. 24:6021-6028(2004).
[28]
INTERACTION WITH UHRF1 AND UHRF2.
PubMed=15361834; DOI=10.1038/sj.onc.1208053;
Unoki M., Nishidate T., Nakamura Y.;
"ICBP90, an E2F-1 target, recruits HDAC1 and binds to methyl-CpG
through its SRA domain.";
Oncogene 23:7601-7610(2004).
[29]
REVIEW ON DEACETYLASE COMPLEXES.
PubMed=10904264; DOI=10.1016/S0168-9525(00)02066-7;
Ahringer J.;
"NuRD and SIN3 histone deacetylase complexes in development.";
Trends Genet. 16:351-356(2000).
[30]
INTERACTION WITH KDM4A.
PubMed=15927959; DOI=10.1074/jbc.M413687200;
Gray S.G., Iglesias A.H., Lizcano F., Villanueva R., Camelo S.,
Jingu H., Teh B.T., Koibuchi N., Chin W.W., Kokkotou E., Dangond F.;
"Functional characterization of JMJD2A, a histone deacetylase- and
retinoblastoma-binding protein.";
J. Biol. Chem. 280:28507-28518(2005).
[31]
INTERACTION WITH BANP.
PubMed=16166625; DOI=10.1128/MCB.25.19.8415-8429.2005;
Rampalli S., Pavithra L., Bhatt A., Kundu T.K., Chattopadhyay S.;
"Tumor suppressor SMAR1 mediates cyclin D1 repression by recruitment
of the SIN3/histone deacetylase 1 complex.";
Mol. Cell. Biol. 25:8415-8429(2005).
[32]
INTERACTION WITH INSM1.
PubMed=16569215; DOI=10.1042/BJ20051669;
Liu W.D., Wang H.W., Muguira M., Breslin M.B., Lan M.S.;
"INSM1 functions as a transcriptional repressor of the neuroD/beta2
gene through the recruitment of cyclin D1 and histone deacetylases.";
Biochem. J. 397:169-177(2006).
[33]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393; SER-421 AND
SER-423, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[34]
INTERACTION WITH SP1, AND FUNCTION.
PubMed=16478997; DOI=10.1128/MCB.26.5.1770-1785.2006;
Hung J.J., Wang Y.T., Chang W.C.;
"Sp1 deacetylation induced by phorbol ester recruits p300 to activate
12(S)-lipoxygenase gene transcription.";
Mol. Cell. Biol. 26:1770-1785(2006).
[35]
FUNCTION, AND INTERACTION WITH BRMS1.
PubMed=17000776; DOI=10.1128/MCB.00940-06;
Liu Y., Smith P.W., Jones D.R.;
"Breast cancer metastasis suppressor 1 functions as a corepressor by
enhancing histone deacetylase 1-mediated deacetylation of RelA/p65 and
promoting apoptosis.";
Mol. Cell. Biol. 26:8683-8696(2006).
[36]
INTERACTION WITH SAP30L.
PubMed=16820529; DOI=10.1093/nar/gkl401;
Viiri K.M., Korkeamaeki H., Kukkonen M.K., Nieminen L.K., Lindfors K.,
Peterson P., Maeki M., Kainulainen H., Lohi O.;
"SAP30L interacts with members of the Sin3A corepressor complex and
targets Sin3A to the nucleolus.";
Nucleic Acids Res. 34:3288-3298(2006).
[37]
INTERACTION WITH PPHLN1.
PubMed=17963697; DOI=10.1016/j.bbrc.2007.10.090;
Kurita M., Suzuki H., Kawano Y., Aiso S., Matsuoka M.;
"CR/periphilin is a transcriptional co-repressor involved in cell
cycle progression.";
Biochem. Biophys. Res. Commun. 364:930-936(2007).
[38]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Prostate cancer;
PubMed=17487921; DOI=10.1002/elps.200600782;
Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
"Toward a global characterization of the phosphoproteome in prostate
cancer cells: identification of phosphoproteins in the LNCaP cell
line.";
Electrophoresis 28:2027-2034(2007).
[39]
INTERACTION WITH SP3.
PubMed=17548428; DOI=10.1096/fj.07-8621com;
Wooten-Blanks L.G., Song P., Senkal C.E., Ogretmen B.;
"Mechanisms of ceramide-mediated repression of the human telomerase
reverse transcriptase promoter via deacetylation of Sp3 by histone
deacetylase 1.";
FASEB J. 21:3386-3397(2007).
[40]
INTERACTION WITH KDM5B.
PubMed=17373667; DOI=10.1002/ijc.22673;
Barrett A., Santangelo S., Tan K., Catchpole S., Roberts K.,
Spencer-Dene B., Hall D., Scibetta A., Burchell J., Verdin E.,
Freemont P., Taylor-Papadimitriou J.;
"Breast cancer associated transcriptional repressor PLU-1/JARID1B
interacts directly with histone deacetylases.";
Int. J. Cancer 121:265-275(2007).
[41]
INTERACTION WITH TRIM28, AND FUNCTION.
PubMed=17704056; DOI=10.1074/jbc.M704757200;
Wang C., Rauscher F.J. III, Cress W.D., Chen J.;
"Regulation of E2F1 function by the nuclear corepressor KAP1.";
J. Biol. Chem. 282:29902-29909(2007).
[42]
INTERACTION WITH DDIT3.
PubMed=17872950; DOI=10.1074/jbc.M703735200;
Ohoka N., Hattori T., Kitagawa M., Onozaki K., Hayashi H.;
"Critical and functional regulation of CHOP (C/EBP homologous protein)
through the N-terminal portion.";
J. Biol. Chem. 282:35687-35694(2007).
[43]
INTERACTION WITH SV40 LARGE T ANTIGEN.
PubMed=17341466; DOI=10.1093/nar/gkl1113;
Valls E., Blanco-Garcia N., Aquizu N., Piedra D., Estaras C.,
de la Cruz X., Martinez-Balbas M.A.;
"Involvement of chromatin and histone deacetylation in SV40 T antigen
transcription regulation.";
Nucleic Acids Res. 35:1958-1968(2007).
[44]
INTERACTION WITH DDX5.
PubMed=17369852; DOI=10.1038/sj.onc.1210387;
Jacobs A.M., Nicol S.M., Hislop R.G., Jaffray E.G., Hay R.T.,
Fuller-Pace F.V.;
"SUMO modification of the DEAD box protein p68 modulates its
transcriptional activity and promotes its interaction with HDAC1.";
Oncogene 26:5866-5876(2007).
[45]
FUNCTION, AND INTERACTION WITH NR1D2.
PubMed=17996965; DOI=10.1016/j.bbamcr.2007.09.004;
Wang J., Liu N., Liu Z., Li Y., Song C., Yuan H., Li Y.Y., Zhao X.,
Lu H.;
"The orphan nuclear receptor Rev-erbbeta recruits Tip60 and HDAC1 to
regulate apolipoprotein CIII promoter.";
Biochim. Biophys. Acta 1783:224-236(2008).
[46]
INTERACTION WITH TRAF6.
PubMed=18093978; DOI=10.1074/jbc.M706307200;
Pham L.V., Zhou H.J., Lin-Lee Y.C., Tamayo A.T., Yoshimura L.C.,
Fu L., Darnay B.G., Ford R.J.;
"Nuclear tumor necrosis factor receptor-associated factor 6 in
lymphoid cells negatively regulates c-Myb-mediated transactivation
through small ubiquitin-related modifier-1 modification.";
J. Biol. Chem. 283:5081-5089(2008).
[47]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[48]
IDENTIFICATION IN A COMPLEX WITH CDYL; MIER1; MIER2 AND HDAC2.
PubMed=19061646; DOI=10.1016/j.molcel.2008.10.025;
Mulligan P., Westbrook T.F., Ottinger M., Pavlova N., Chang B.,
Macia E., Shi Y.J., Barretina J., Liu J., Howley P.M., Elledge S.J.,
Shi Y.;
"CDYL bridges REST and histone methyltransferases for gene repression
and suppression of cellular transformation.";
Mol. Cell 32:718-726(2008).
[49]
METHYLATION AT LYS-432.
PubMed=18438403; DOI=10.1038/nchembio.88;
Rathert P., Dhayalan A., Murakami M., Zhang X., Tamas R.,
Jurkowska R., Komatsu Y., Shinkai Y., Cheng X., Jeltsch A.;
"Protein lysine methyltransferase G9a acts on non-histone targets.";
Nat. Chem. Biol. 4:344-346(2008).
[50]
FUNCTION, AND INTERACTION WITH RB1 AND SMARCA4/BRG1.
PubMed=19081374; DOI=10.1016/j.neuron.2008.09.040;
Qiu Z., Ghosh A.;
"A calcium-dependent switch in a CREST-BRG1 complex regulates
activity-dependent gene expression.";
Neuron 60:775-787(2008).
[51]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[52]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421 AND SER-423, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=18318008; DOI=10.1002/pmic.200700884;
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
Zou H., Gu J.;
"Large-scale phosphoproteome analysis of human liver tissue by
enrichment and fractionation of phosphopeptides with strong anion
exchange chromatography.";
Proteomics 8:1346-1361(2008).
[53]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[54]
INTERACTION WITH PRDM16 AND SMAD3.
PubMed=19049980; DOI=10.1074/jbc.M808989200;
Takahata M., Inoue Y., Tsuda H., Imoto I., Koinuma D., Hayashi M.,
Ichikura T., Yamori T., Nagasaki K., Yoshida M., Matsuoka M.,
Morishita K., Yuki K., Hanyu A., Miyazawa K., Inazawa J., Miyazono K.,
Imamura T.;
"SKI and MEL1 cooperate to inhibit transforming growth factor-beta
signal in gastric cancer cells.";
J. Biol. Chem. 284:3334-3344(2009).
[55]
FUNCTION, INTERACTION WITH TSHZ3, AND IDENTIFICATION IN A TRIMERIC
COMPLEX WITH APBB1 AND TSHZ3.
PubMed=19343227; DOI=10.1371/journal.pone.0005071;
Kajiwara Y., Akram A., Katsel P., Haroutunian V., Schmeidler J.,
Beecham G., Haines J.L., Pericak-Vance M.A., Buxbaum J.D.;
"FE65 binds Teashirt, inhibiting expression of the primate-specific
caspase-4.";
PLoS ONE 4:E5071-E5071(2009).
[56]
UBIQUITINATION, INTERACTION WITH CHFR, AND MUTAGENESIS OF HIS-141;
PHE-287 AND MET-297.
PubMed=19182791; DOI=10.1038/ncb1837;
Oh Y.M., Kwon Y.E., Kim J.M., Bae S.J., Lee B.K., Yoo S.J.,
Chung C.H., Deshaies R.J., Seol J.H.;
"Chfr is linked to tumour metastasis through the downregulation of
HDAC1.";
Nat. Cell Biol. 11:295-302(2009).
[57]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393 AND SER-421, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[58]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-74 AND LYS-220, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[59]
INTERACTION WITH CCAR2.
PubMed=21030595; DOI=10.1074/jbc.M110.153270;
Chini C.C., Escande C., Nin V., Chini E.N.;
"HDAC3 is negatively regulated by the nuclear protein DBC1.";
J. Biol. Chem. 285:40830-40837(2010).
[60]
UBIQUITINATION BY KCTD11.
PubMed=20081843; DOI=10.1038/ncb2013;
Canettieri G., Di Marcotullio L., Greco A., Coni S., Antonucci L.,
Infante P., Pietrosanti L., De Smaele E., Ferretti E., Miele E.,
Pelloni M., De Simone G., Pedone E.M., Gallinari P., Giorgi A.,
Steinkuhler C., Vitagliano L., Pedone C., Schinin M.E., Screpanti I.,
Gulino A.;
"Histone deacetylase and Cullin3-REN(KCTD11) ubiquitin ligase
interplay regulates Hedgehog signalling through Gli acetylation.";
Nat. Cell Biol. 12:132-142(2010).
[61]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393; SER-421 AND
SER-423, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[62]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[63]
INTERACTION WITH SMARCAD1.
PubMed=21549307; DOI=10.1016/j.molcel.2011.02.036;
Rowbotham S.P., Barki L., Neves-Costa A., Santos F., Dean W.,
Hawkes N., Choudhary P., Will W.R., Webster J., Oxley D., Green C.M.,
Varga-Weisz P., Mermoud J.E.;
"Maintenance of silent chromatin through replication requires SWI/SNF-
like chromatin remodeler SMARCAD1.";
Mol. Cell 42:285-296(2011).
[64]
INTERACTION WITH BHLHE40.
PubMed=21829689; DOI=10.1371/journal.pone.0023046;
Hong Y., Xing X., Li S., Bi H., Yang C., Zhao F., Liu Y., Ao X.,
Chang A.K., Wu H.;
"SUMOylation of DEC1 protein regulates its transcriptional activity
and enhances its stability.";
PLoS ONE 6:E23046-E23046(2011).
[65]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393; SER-421 AND
SER-423, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[66]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393; SER-409; SER-421
AND SER-423, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[67]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[68]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-444; LYS-457 AND LYS-476,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[69]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-476, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[70]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-444 AND LYS-476, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to
replication stress reveals novel small ubiquitin-like modified target
proteins and acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[71]
INTERACTION WITH DNTTIP1, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=25653165; DOI=10.1093/nar/gkv068;
Itoh T., Fairall L., Muskett F.W., Milano C.P., Watson P.J.,
Arnaudo N., Saleh A., Millard C.J., El-Mezgueldi M., Martino F.,
Schwabe J.W.;
"Structural and functional characterization of a cell cycle associated
HDAC1/2 complex reveals the structural basis for complex assembly and
nucleosome targeting.";
Nucleic Acids Res. 43:2033-2044(2015).
[72]
INTERACTION WITH CHD4.
PubMed=27616479; DOI=10.1016/j.ajhg.2016.08.001;
DDD Study;
Weiss K., Terhal P.A., Cohen L., Bruccoleri M., Irving M.,
Martinez A.F., Rosenfeld J.A., Machol K., Yang Y., Liu P.,
Walkiewicz M., Beuten J., Gomez-Ospina N., Haude K., Fong C.T.,
Enns G.M., Bernstein J.A., Fan J., Gotway G., Ghorbani M.,
van Gassen K., Monroe G.R., van Haaften G., Basel-Vanagaite L.,
Yang X.J., Campeau P.M., Muenke M.;
"De novo mutations in CHD4, an ATP-dependent chromatin remodeler gene,
cause an intellectual disability syndrome with distinctive
dysmorphisms.";
Am. J. Hum. Genet. 99:934-941(2016).
[73]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-438; LYS-476 AND LYS-480,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
-!- FUNCTION: Responsible for the deacetylation of lysine residues on
the N-terminal part of the core histones (H2A, H2B, H3 and H4).
Histone deacetylation gives a tag for epigenetic repression and
plays an important role in transcriptional regulation, cell cycle
progression and developmental events. Histone deacetylases act via
the formation of large multiprotein complexes. Deacetylates SP
proteins, SP1 and SP3, and regulates their function. Component of
the BRG1-RB1-HDAC1 complex, which negatively regulates the CREST-
mediated transcription in resting neurons. Upon calcium
stimulation, HDAC1 is released from the complex and CREBBP is
recruited, which facilitates transcriptional activation.
Deacetylates TSHZ3 and regulates its transcriptional repressor
activity. Deacetylates 'Lys-310' in RELA and thereby inhibits the
transcriptional activity of NF-kappa-B. Deacetylates NR1D2 and
abrogates the effect of KAT5-mediated relieving of NR1D2
transcription repression activity. Component of a
RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone
deacetylase (HDAC) recruitment, a number of genes implicated in
multilineage blood cell development. Involved in CIART-mediated
transcriptional repression of the circadian transcriptional
activator: CLOCK-ARNTL/BMAL1 heterodimer. Required for the
transcriptional repression of circadian target genes, such as
PER1, mediated by the large PER complex or CRY1 through histone
deacetylation. {ECO:0000269|PubMed:12837748,
ECO:0000269|PubMed:16478997, ECO:0000269|PubMed:17000776,
ECO:0000269|PubMed:17704056, ECO:0000269|PubMed:17996965,
ECO:0000269|PubMed:19081374, ECO:0000269|PubMed:19343227}.
-!- CATALYTIC ACTIVITY: Hydrolysis of an N(6)-acetyl-lysine residue of
a histone to yield a deacetylated histone.
-!- SUBUNIT: Part of the core histone deacetylase (HDAC) complex
composed of HDAC1, HDAC2, RBBP4 and RBBP7. The core complex
associates with MTA2, MBD2, MBD3, MTA1L1, CHD3 and CHD4 to form
the nucleosome remodeling and histone deacetylation (NuRD)
complex, or with SIN3, SAP18 and SAP30 to form the SIN3 HDAC
complex. Component of a BHC histone deacetylase complex that
contains HDAC1, HDAC2, HMG20B/BRAF35, KDM1A, RCOR1/CoREST and
PHF21A/BHC80. The BHC complex may also contain ZMYM2, ZNF217,
ZMYM3, GSE1 and GTF2I. Component of a mSin3A corepressor complex
that contains SIN3A, SAP130, SUDS3/SAP45, ARID4B/SAP180, HDAC1 and
HDAC2. Found in a trimeric complex with APBB1 and TSHZ3; the
interaction between HDAC1 and APBB1 is mediated by TSHZ3.
Component of a RCOR/GFI/KDM1A/HDAC complex. Part of a complex
composed of TRIM28, HDAC1, HDAC2 and EHMT2. Part of a complex
containing at least CDYL, MIER1, MIER2, HDAC1 and HDAC2. The large
PER complex involved in the histone deacetylation is composed of
at least HDAC1, PER2, SFPQ and SIN3A. Associates with the 9-1-1
complex; interacts with HUS1. Found in a complex with DNMT3A and
HDAC7. Interacts with the non-histone region of H2AFY. Interacts
with TRIM28; the interaction recruits HDAC1 to E2F1 and inhibits
its acetylation. Interacts with SP1; the interaction deacetylates
SP1 and regulates its transcriptional activity. Interacts with
SP3; the interaction deacetylates SP3 and regulates its
transcriptional activity. In vitro, C(18) ceramides increase this
interaction and the subsequent SP3 deacetylation and SP3-mediated
repression of the TERT promoter. Interacts with TSHZ3 (via N-
terminus); the interaction is direct. Interacts with APEX1; the
interaction is not dependent on the acetylated status of APEX1.
Interacts with C10orf90/FATS (via its N-terminal); the interaction
prevents binding of HDAC1 to CDKN1A/p21 and facilitates the
acetylation and stabilization of CDKN1A/p21. Interacts with
CDKN1A/p21. Interacts with CDK5 complexed to CDK5R1 (p25).
Interacts directly with GFI1 and GFI1B. Interacts with NR1D2 (via
C-terminus). Interacts with TSC22D3 isoform 1; this interaction
affects HDAC1 activity on MYOG promoter and thus inhibits MYOD1
transcriptional activity. Interacts with BAZ2A/TIP5, BANP, BCL6,
BCOR, BHLHE40/DEC1, BRMS1, BRMS1L, CBFA2T3, CHFR, CIART, CRY1,
DAXX, DDIT3/CHOP, DDX5, DNMT1, E4F1, EP300, HCFC1, HDAC9, INSM1,
NFE4, NR4A2/NURR1, MIER1, KDM4A, KDM5B, KLF1, MINT, NRIP1, PCAF,
PHB2, PRDM6, PRDM16, RB1, RERE, SAMSN1, SAP30L, SETDB1, SMAD3,
SMARCA4/BRG1, SMYD2, SUV39H1, TGIF, TGIF2, TRAF6, UHRF1, UHRF2,
ZMYND15, ZNF431 and ZNF541. Interacts with KDM5A (By similarity).
Interacts with DNTTIP1 (PubMed:25653165). Identified in a histone
deacetylase complex that contains DNTTIP1, HDAC1 and ELMSAN1; this
complex assembles into a tetramer that contains four copies of
each protein chain (PubMed:25653165). Interacts with CCAR2
(PubMed:21030595). Interacts with PPHLN1 (PubMed:17963697). Found
in a complex with YY1, SIN3A and GON4L (By similarity). Interacts
with CHD4 (PubMed:27616479). Found in a complex composed of at
least SINHCAF, SIN3A, HDAC1, SAP30, RBBP4, OGT and TET1. Interacts
with SIN3A (By similarity). {ECO:0000250|UniProtKB:O09106,
ECO:0000269|PubMed:10487760, ECO:0000269|PubMed:10655483,
ECO:0000269|PubMed:10669754, ECO:0000269|PubMed:10846170,
ECO:0000269|PubMed:10898795, ECO:0000269|PubMed:11006275,
ECO:0000269|PubMed:11102443, ECO:0000269|PubMed:11331609,
ECO:0000269|PubMed:11427533, ECO:0000269|PubMed:11533236,
ECO:0000269|PubMed:12482978, ECO:0000269|PubMed:12493763,
ECO:0000269|PubMed:12670868, ECO:0000269|PubMed:12724404,
ECO:0000269|PubMed:12730668, ECO:0000269|PubMed:12837748,
ECO:0000269|PubMed:14633989, ECO:0000269|PubMed:15273251,
ECO:0000269|PubMed:15361834, ECO:0000269|PubMed:15451426,
ECO:0000269|PubMed:15454082, ECO:0000269|PubMed:15927959,
ECO:0000269|PubMed:16166625, ECO:0000269|PubMed:16478997,
ECO:0000269|PubMed:16569215, ECO:0000269|PubMed:16820529,
ECO:0000269|PubMed:17000776, ECO:0000269|PubMed:17341466,
ECO:0000269|PubMed:17369852, ECO:0000269|PubMed:17373667,
ECO:0000269|PubMed:17548428, ECO:0000269|PubMed:17704056,
ECO:0000269|PubMed:17872950, ECO:0000269|PubMed:17963697,
ECO:0000269|PubMed:17996965, ECO:0000269|PubMed:18093978,
ECO:0000269|PubMed:19049980, ECO:0000269|PubMed:19061646,
ECO:0000269|PubMed:19081374, ECO:0000269|PubMed:19182791,
ECO:0000269|PubMed:19343227, ECO:0000269|PubMed:21030595,
ECO:0000269|PubMed:21549307, ECO:0000269|PubMed:21829689,
ECO:0000269|PubMed:25653165, ECO:0000269|PubMed:27616479}.
-!- INTERACTION:
Q9UKG1:APPL1; NbExp=2; IntAct=EBI-301834, EBI-741243;
Q14865:ARID5B; NbExp=5; IntAct=EBI-301834, EBI-1210388;
Q9C0K0:BCL11B; NbExp=3; IntAct=EBI-301834, EBI-6597578;
P29128:BICP0 (xeno); NbExp=2; IntAct=EBI-301834, EBI-11292028;
Q9HCU9:BRMS1; NbExp=4; IntAct=EBI-301834, EBI-714781;
Q6PH81:C16orf87; NbExp=3; IntAct=EBI-301834, EBI-6598617;
Q14839:CHD4; NbExp=6; IntAct=EBI-301834, EBI-372916;
P68400:CSNK2A1; NbExp=2; IntAct=EBI-301834, EBI-347804;
Q9UER7:DAXX; NbExp=2; IntAct=EBI-301834, EBI-77321;
Q92841-4:DDX17; NbExp=3; IntAct=EBI-301834, EBI-5280703;
P17844:DDX5; NbExp=4; IntAct=EBI-301834, EBI-351962;
Q7L2E3:DHX30; NbExp=3; IntAct=EBI-301834, EBI-1211456;
Q9UJW3:DNMT3L; NbExp=3; IntAct=EBI-301834, EBI-740967;
Q01094:E2F1; NbExp=2; IntAct=EBI-301834, EBI-448924;
Q66K89:E4F1; NbExp=3; IntAct=EBI-301834, EBI-1227043;
Q96KQ7:EHMT2; NbExp=7; IntAct=EBI-301834, EBI-744366;
Q96D98:EID2B; NbExp=2; IntAct=EBI-301834, EBI-724968;
Q9NP50:FAM60A; NbExp=5; IntAct=EBI-301834, EBI-741906;
Q99684:GFI1; NbExp=4; IntAct=EBI-301834, EBI-949368;
Q13227:GPS2; NbExp=2; IntAct=EBI-301834, EBI-713355;
P51610:HCFC1; NbExp=2; IntAct=EBI-301834, EBI-396176;
Q92769:HDAC2; NbExp=12; IntAct=EBI-301834, EBI-301821;
P62805:HIST2H4B; NbExp=3; IntAct=EBI-301834, EBI-302023;
Q9Y4K0:LOXL2; NbExp=2; IntAct=EBI-301834, EBI-7172227;
P43355:MAGEA1; NbExp=2; IntAct=EBI-301834, EBI-740978;
Q9UIS9:MBD1; NbExp=2; IntAct=EBI-301834, EBI-867196;
O95983:MBD3; NbExp=6; IntAct=EBI-301834, EBI-1783068;
Q8N108:MIER1; NbExp=7; IntAct=EBI-301834, EBI-3504940;
Q13330:MTA1; NbExp=10; IntAct=EBI-301834, EBI-714236;
O94776:MTA2; NbExp=9; IntAct=EBI-301834, EBI-1783035;
Q9Y618:NCOR2; NbExp=2; IntAct=EBI-301834, EBI-80830;
P19838:NFKB1; NbExp=5; IntAct=EBI-301834, EBI-300010;
P06748:NPM1; NbExp=2; IntAct=EBI-301834, EBI-78579;
Q15466:NR0B2; NbExp=2; IntAct=EBI-301834, EBI-3910729;
Q9Y5X4:NR2E3; NbExp=2; IntAct=EBI-301834, EBI-7216962;
Q9NQX1:PRDM5; NbExp=3; IntAct=EBI-301834, EBI-4292031;
Q96N64:PWWP2A; NbExp=5; IntAct=EBI-301834, EBI-6597774;
P06400:RB1; NbExp=15; IntAct=EBI-301834, EBI-491274;
Q09028:RBBP4; NbExp=7; IntAct=EBI-301834, EBI-620823;
Q16576:RBBP7; NbExp=7; IntAct=EBI-301834, EBI-352227;
Q9UKL0:RCOR1; NbExp=10; IntAct=EBI-301834, EBI-926563;
Q04206:RELA; NbExp=6; IntAct=EBI-301834, EBI-73886;
O00422:SAP18; NbExp=2; IntAct=EBI-301834, EBI-1044156;
Q96ST3:SIN3A; NbExp=7; IntAct=EBI-301834, EBI-347218;
O95863:SNAI1; NbExp=3; IntAct=EBI-301834, EBI-1045459;
P08047:SP1; NbExp=2; IntAct=EBI-301834, EBI-298336;
O43463:SUV39H1; NbExp=3; IntAct=EBI-301834, EBI-349968;
P04637:TP53; NbExp=7; IntAct=EBI-301834, EBI-366083;
O95365:ZBTB7A; NbExp=2; IntAct=EBI-301834, EBI-2795384;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10846170}.
-!- TISSUE SPECIFICITY: Ubiquitous, with higher levels in heart,
pancreas and testis, and lower levels in kidney and brain.
-!- PTM: Sumoylated on Lys-444 and Lys-476; which promotes enzymatic
activity. Desumoylated by SENP1. {ECO:0000269|PubMed:11960997,
ECO:0000269|PubMed:12032081, ECO:0000269|PubMed:15199155}.
-!- PTM: Phosphorylation on Ser-421 and Ser-423 promotes enzymatic
activity and interactions with NuRD and SIN3 complexes.
Phosphorylated by CDK5. {ECO:0000269|PubMed:11602581}.
-!- PTM: Ubiquitinated by CHFR, leading to its degradation by the
proteasome. Ubiquitinated by KCTD11, leading to proteasomal
degradation. {ECO:0000269|PubMed:19182791,
ECO:0000269|PubMed:20081843}.
-!- SIMILARITY: Belongs to the histone deacetylase family. HD type 1
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U50079; AAC50475.1; -; mRNA.
EMBL; D50405; BAA08909.1; -; mRNA.
EMBL; BC000301; AAH00301.1; -; mRNA.
CCDS; CCDS360.1; -.
RefSeq; NP_004955.2; NM_004964.2.
UniGene; Hs.88556; -.
PDB; 1TYI; Model; -; A=1-482.
PDB; 4BKX; X-ray; 3.00 A; B=1-482.
PDB; 5ICN; X-ray; 3.30 A; B=1-376.
PDBsum; 1TYI; -.
PDBsum; 4BKX; -.
PDBsum; 5ICN; -.
ProteinModelPortal; Q13547; -.
SMR; Q13547; -.
BioGrid; 109315; 560.
CORUM; Q13547; -.
DIP; DIP-24184N; -.
IntAct; Q13547; 262.
MINT; MINT-90475; -.
STRING; 9606.ENSP00000362649; -.
BindingDB; Q13547; -.
ChEMBL; CHEMBL325; -.
DrugBank; DB05015; Belinostat.
DrugBank; DB05921; CRA-024781.
DrugBank; DB05651; MGCD-0103.
DrugBank; DB06603; Panobinostat.
DrugBank; DB06176; Romidepsin.
DrugBank; DB05223; SB939.
DrugBank; DB02546; Vorinostat.
GuidetoPHARMACOLOGY; 2658; -.
iPTMnet; Q13547; -.
PhosphoSitePlus; Q13547; -.
SwissPalm; Q13547; -.
BioMuta; HDAC1; -.
DMDM; 2498443; -.
EPD; Q13547; -.
PaxDb; Q13547; -.
PeptideAtlas; Q13547; -.
PRIDE; Q13547; -.
TopDownProteomics; Q13547; -.
DNASU; 3065; -.
Ensembl; ENST00000373548; ENSP00000362649; ENSG00000116478.
GeneID; 3065; -.
KEGG; hsa:3065; -.
CTD; 3065; -.
DisGeNET; 3065; -.
EuPathDB; HostDB:ENSG00000116478.11; -.
GeneCards; HDAC1; -.
HGNC; HGNC:4852; HDAC1.
HPA; CAB005017; -.
HPA; CAB068191; -.
HPA; HPA029693; -.
MIM; 601241; gene.
neXtProt; NX_Q13547; -.
OpenTargets; ENSG00000116478; -.
PharmGKB; PA29226; -.
eggNOG; KOG1342; Eukaryota.
eggNOG; COG0123; LUCA.
GeneTree; ENSGT00530000062889; -.
HOGENOM; HOG000225180; -.
HOVERGEN; HBG057112; -.
InParanoid; Q13547; -.
KO; K06067; -.
OMA; QNTNDYL; -.
OrthoDB; EOG091G067J; -.
PhylomeDB; Q13547; -.
TreeFam; TF106171; -.
BRENDA; 3.5.1.98; 2681.
Reactome; R-HSA-1362277; Transcription of E2F targets under negative control by DREAM complex.
Reactome; R-HSA-1362300; Transcription of E2F targets under negative control by p107 (RBL1) and p130 (RBL2) in complex with HDAC1.
Reactome; R-HSA-1538133; G0 and Early G1.
Reactome; R-HSA-193670; p75NTR negatively regulates cell cycle via SC1.
Reactome; R-HSA-201722; Formation of the beta-catenin:TCF transactivating complex.
Reactome; R-HSA-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
Reactome; R-HSA-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
Reactome; R-HSA-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
Reactome; R-HSA-2644606; Constitutive Signaling by NOTCH1 PEST Domain Mutants.
Reactome; R-HSA-2894862; Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
Reactome; R-HSA-3214815; HDACs deacetylate histones.
Reactome; R-HSA-3769402; Deactivation of the beta-catenin transactivating complex.
Reactome; R-HSA-427389; ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression.
Reactome; R-HSA-427413; NoRC negatively regulates rRNA expression.
Reactome; R-HSA-4551638; SUMOylation of chromatin organization proteins.
Reactome; R-HSA-4641265; Repression of WNT target genes.
Reactome; R-HSA-539107; Activation of E2F1 target genes at G1/S.
Reactome; R-HSA-6804758; Regulation of TP53 Activity through Acetylation.
Reactome; R-HSA-73762; RNA Polymerase I Transcription Initiation.
Reactome; R-HSA-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
Reactome; R-HSA-8943724; Regulation of PTEN gene transcription.
Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production.
SABIO-RK; Q13547; -.
SIGNOR; Q13547; -.
ChiTaRS; HDAC1; human.
GeneWiki; HDAC1; -.
GenomeRNAi; 3065; -.
PRO; PR:Q13547; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000116478; -.
CleanEx; HS_HDAC1; -.
ExpressionAtlas; Q13547; baseline and differential.
Genevisible; Q13547; HS.
GO; GO:0000785; C:chromatin; IDA:ParkinsonsUK-UCL.
GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0000118; C:histone deacetylase complex; TAS:UniProtKB.
GO; GO:0000790; C:nuclear chromatin; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0016581; C:NuRD complex; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IDA:UniProtKB.
GO; GO:0016580; C:Sin3 complex; IDA:BHF-UCL.
GO; GO:0033613; F:activating transcription factor binding; IPI:UniProtKB.
GO; GO:0001047; F:core promoter binding; IDA:UniProtKB.
GO; GO:0001046; F:core promoter sequence-specific DNA binding; IDA:CAFA.
GO; GO:0019213; F:deacetylase activity; ISS:UniProtKB.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0004407; F:histone deacetylase activity; IDA:BHF-UCL.
GO; GO:0042826; F:histone deacetylase binding; IPI:UniProtKB.
GO; GO:0032041; F:NAD-dependent histone deacetylase activity (H3-K14 specific); IEA:UniProtKB-EC.
GO; GO:0051059; F:NF-kappaB binding; IPI:UniProtKB.
GO; GO:0002039; F:p53 binding; IPI:CAFA.
GO; GO:0033558; F:protein deacetylase activity; IDA:UniProtKB.
GO; GO:0047485; F:protein N-terminus binding; IDA:MGI.
GO; GO:0070491; F:repressing transcription factor binding; IPI:ParkinsonsUK-UCL.
GO; GO:0001103; F:RNA polymerase II repressing transcription factor binding; IPI:BHF-UCL.
GO; GO:0001106; F:RNA polymerase II transcription corepressor activity; IDA:BHF-UCL.
GO; GO:0001085; F:RNA polymerase II transcription factor binding; IPI:ParkinsonsUK-UCL.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; TAS:ProtInc.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:ParkinsonsUK-UCL.
GO; GO:0000976; F:transcription regulatory region sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0043044; P:ATP-dependent chromatin remodeling; IDA:UniProtKB.
GO; GO:1904837; P:beta-catenin-TCF complex assembly; TAS:Reactome.
GO; GO:0007596; P:blood coagulation; TAS:Reactome.
GO; GO:0006325; P:chromatin organization; TAS:UniProtKB.
GO; GO:0006338; P:chromatin remodeling; IC:BHF-UCL.
GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
GO; GO:0042733; P:embryonic digit morphogenesis; ISS:BHF-UCL.
GO; GO:0009913; P:epidermal cell differentiation; ISS:BHF-UCL.
GO; GO:0061029; P:eyelid development in camera-type eye; ISS:BHF-UCL.
GO; GO:0061198; P:fungiform papilla formation; ISS:BHF-UCL.
GO; GO:0060789; P:hair follicle placode formation; ISS:BHF-UCL.
GO; GO:0016575; P:histone deacetylation; IMP:UniProtKB.
GO; GO:0070932; P:histone H3 deacetylation; IDA:BHF-UCL.
GO; GO:0070933; P:histone H4 deacetylation; IDA:BHF-UCL.
GO; GO:0006346; P:methylation-dependent chromatin silencing; IGI:BHF-UCL.
GO; GO:0043922; P:negative regulation by host of viral transcription; IMP:UniProtKB.
GO; GO:0060766; P:negative regulation of androgen receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0043066; P:negative regulation of apoptotic process; ISS:BHF-UCL.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IGI:ParkinsonsUK-UCL.
GO; GO:0010629; P:negative regulation of gene expression; IMP:CACAO.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
GO; GO:0042475; P:odontogenesis of dentin-containing tooth; ISS:BHF-UCL.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:BHF-UCL.
GO; GO:0010870; P:positive regulation of receptor biosynthetic process; IMP:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:BHF-UCL.
GO; GO:0006476; P:protein deacetylation; IDA:UniProtKB.
GO; GO:0045652; P:regulation of megakaryocyte differentiation; TAS:Reactome.
GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
Gene3D; 3.40.800.20; -; 1.
InterPro; IPR000286; His_deacetylse.
InterPro; IPR003084; His_deacetylse_1.
InterPro; IPR023801; His_deacetylse_dom.
InterPro; IPR037138; His_deacetylse_dom_sf.
InterPro; IPR023696; Ureohydrolase_dom_sf.
PANTHER; PTHR10625; PTHR10625; 1.
Pfam; PF00850; Hist_deacetyl; 1.
PIRSF; PIRSF037913; His_deacetylse_1; 1.
PRINTS; PR01270; HDASUPER.
PRINTS; PR01271; HISDACETLASE.
SUPFAM; SSF52768; SSF52768; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Biological rhythms; Chromatin regulator;
Complete proteome; Host-virus interaction; Hydrolase; Isopeptide bond;
Methylation; Nucleus; Phosphoprotein; Reference proteome; Repressor;
S-nitrosylation; Transcription; Transcription regulation;
Ubl conjugation.
CHAIN 1 482 Histone deacetylase 1.
/FTId=PRO_0000114687.
REGION 9 321 Histone deacetylase.
ACT_SITE 141 141
MOD_RES 74 74 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 220 220 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 261 261 S-nitrosocysteine.
{ECO:0000250|UniProtKB:P70288}.
MOD_RES 273 273 S-nitrosocysteine.
{ECO:0000250|UniProtKB:P70288}.
MOD_RES 393 393 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:17487921,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 406 406 Phosphoserine.
{ECO:0000250|UniProtKB:Q92769}.
MOD_RES 409 409 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 421 421 Phosphoserine; by CK2.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18318008,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:11602581}.
MOD_RES 423 423 Phosphoserine; by CK2.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18318008,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:11602581}.
MOD_RES 432 432 N6-methylated lysine; by EHMT2.
{ECO:0000269|PubMed:18438403}.
CROSSLNK 74 74 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:Q92769}.
CROSSLNK 438 438 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 444 444 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate. {ECO:0000269|PubMed:11960997}.
CROSSLNK 444 444 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297}.
CROSSLNK 456 456 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q92769}.
CROSSLNK 457 457 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447}.
CROSSLNK 473 473 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q92769}.
CROSSLNK 476 476 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate. {ECO:0000269|PubMed:11960997}.
CROSSLNK 476 476 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 480 480 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
MUTAGEN 141 141 H->A: Abolishes histone deacetylase
activity. {ECO:0000269|PubMed:19182791}.
MUTAGEN 287 287 F->Y: Abolishes interaction with CHFR;
when associated with I-297.
{ECO:0000269|PubMed:19182791}.
MUTAGEN 297 297 M->I: Abolishes interaction with CHFR;
when associated with Y-287.
{ECO:0000269|PubMed:19182791}.
MUTAGEN 391 482 Missing: Strongly decreases deacetylase
activity, and disrupts interaction with
NuRD and SIN3 complexes.
MUTAGEN 421 421 S->A: Strongly decreases deacetylase
activity, and disrupts interaction with
NuRD and SIN3 complexes.
{ECO:0000269|PubMed:11602581}.
MUTAGEN 421 421 S->D,E: Slightly decreases deacetylase
activity. {ECO:0000269|PubMed:11602581}.
MUTAGEN 423 423 S->A: Strongly decreases deacetylase
activity, and disrupts interaction with
NuRD and SIN3 complexes.
{ECO:0000269|PubMed:11602581}.
MUTAGEN 423 423 S->D,E: Decreases deacetylase activity.
{ECO:0000269|PubMed:11602581}.
MUTAGEN 424 424 E->A: Slightly decreases deacetylase
activity, no effect on interaction with
NuRD and SIN3 complexes.
MUTAGEN 425 425 E->A: No effect on deacetylase activity,
no effect on interaction with NuRD and
SIN3 complexes.
MUTAGEN 426 426 E->A: Decreases deacetylase activity, and
disrupts interaction with NuRD and SIN3
complexes.
CONFLICT 312 312 W -> R (in Ref. 2; BAA08909).
{ECO:0000305}.
STRAND 11 14 {ECO:0000244|PDB:4BKX}.
HELIX 19 21 {ECO:0000244|PDB:4BKX}.
HELIX 33 44 {ECO:0000244|PDB:4BKX}.
TURN 45 47 {ECO:0000244|PDB:5ICN}.
HELIX 48 50 {ECO:0000244|PDB:4BKX}.
STRAND 51 56 {ECO:0000244|PDB:4BKX}.
HELIX 61 64 {ECO:0000244|PDB:4BKX}.
TURN 65 67 {ECO:0000244|PDB:4BKX}.
HELIX 70 78 {ECO:0000244|PDB:4BKX}.
TURN 83 86 {ECO:0000244|PDB:4BKX}.
HELIX 88 94 {ECO:0000244|PDB:4BKX}.
TURN 97 99 {ECO:0000244|PDB:4BKX}.
HELIX 106 125 {ECO:0000244|PDB:4BKX}.
STRAND 130 136 {ECO:0000244|PDB:4BKX}.
STRAND 151 153 {ECO:0000244|PDB:4BKX}.
HELIX 155 163 {ECO:0000244|PDB:4BKX}.
TURN 164 166 {ECO:0000244|PDB:4BKX}.
STRAND 170 174 {ECO:0000244|PDB:4BKX}.
STRAND 176 178 {ECO:0000244|PDB:4BKX}.
HELIX 181 186 {ECO:0000244|PDB:4BKX}.
TURN 187 189 {ECO:0000244|PDB:4BKX}.
STRAND 191 200 {ECO:0000244|PDB:4BKX}.
STRAND 205 207 {ECO:0000244|PDB:4BKX}.
HELIX 217 219 {ECO:0000244|PDB:4BKX}.
STRAND 223 228 {ECO:0000244|PDB:4BKX}.
HELIX 234 252 {ECO:0000244|PDB:4BKX}.
STRAND 255 260 {ECO:0000244|PDB:4BKX}.
HELIX 263 265 {ECO:0000244|PDB:4BKX}.
HELIX 278 289 {ECO:0000244|PDB:4BKX}.
STRAND 295 298 {ECO:0000244|PDB:4BKX}.
HELIX 305 319 {ECO:0000244|PDB:4BKX}.
HELIX 334 336 {ECO:0000244|PDB:4BKX}.
TURN 338 340 {ECO:0000244|PDB:4BKX}.
HELIX 356 371 {ECO:0000244|PDB:4BKX}.
SEQUENCE 482 AA; 55103 MW; 4D35B7C1ED7838D6 CRC64;
MAQTQGTRRK VCYYYDGDVG NYYYGQGHPM KPHRIRMTHN LLLNYGLYRK MEIYRPHKAN
AEEMTKYHSD DYIKFLRSIR PDNMSEYSKQ MQRFNVGEDC PVFDGLFEFC QLSTGGSVAS
AVKLNKQQTD IAVNWAGGLH HAKKSEASGF CYVNDIVLAI LELLKYHQRV LYIDIDIHHG
DGVEEAFYTT DRVMTVSFHK YGEYFPGTGD LRDIGAGKGK YYAVNYPLRD GIDDESYEAI
FKPVMSKVME MFQPSAVVLQ CGSDSLSGDR LGCFNLTIKG HAKCVEFVKS FNLPMLMLGG
GGYTIRNVAR CWTYETAVAL DTEIPNELPY NDYFEYFGPD FKLHISPSNM TNQNTNEYLE
KIKQRLFENL RMLPHAPGVQ MQAIPEDAIP EESGDEDEDD PDKRISICSS DKRIACEEEF
SDSEEEGEGG RKNSSNFKKA KRVKTEDEKE KDPEEKKEVT EEEKTKEEKP EAKGVKEEVK
LA


Related products :

Catalog number Product name Quantity
AHP1420 RABBIT ANTI HISTONE DEACETYLASE 1, Product Type Polyclonal Antibody, Specificity HISTONE DEACETYLASE 1, Target Species Human, Host Rabbit, Format Purified, Isotypes Polyclonal IgG, Applications 50 µg
SCH-AHP1420 RABBIT ANTI HISTONE DEACETYLASE 1, Product Type Polyclonal Antibody, Specificity HISTONE DEACETYLASE 1, Target Species Human, Host Rabbit, Format Purified, Isotypes Polyclonal IgG, Applications 50 µg
AHP596 RABBIT ANTI HISTONE DEACETYLASE 3, Product Type Polyclonal Antibody, Specificity HISTONE DEACETYLASE 3, Target Species Human, Host Rabbit, Format Purified, Isotypes Polyclonal IgG, Applications 50 µg
SCH-AHP596 RABBIT ANTI HISTONE DEACETYLASE 3, Product Type Polyclonal Antibody, Specificity HISTONE DEACETYLASE 3, Target Species Human, Host Rabbit, Format Purified, Isotypes Polyclonal IgG, Applications 50 µg
AHP595 RABBIT ANTI HUMAN HISTONE DEACETYLASE 1, Product Type Polyclonal Antibody, Specificity HISTONE DEACETYLASE 1, Target Species Human, Host Rabbit, Format Purified, Isotypes Polyclonal IgG, Applica 50 µg
SCH-AHP595 RABBIT ANTI HUMAN HISTONE DEACETYLASE 1, Product Type Polyclonal Antibody, Specificity HISTONE DEACETYLASE 1, Target Species Human, Host Rabbit, Format Purified, Isotypes Polyclonal IgG, Applica 50 µg
MCA3660Z MOUSE ANTI HUMAN HISTONE DEACETYLASE 5 Azide Free, Product Type Monoclonal Antibody, Specificity HISTONE DEACETYLASE 5, Target Species Human, Host Mouse, Format Azide Free, Isotypes IgG1, Applic 0.1 mg
MCA5048Z MOUSE ANTI HUMAN HISTONE DEACETYLASE 4 Azide free, Product Type Monoclonal Antibody, Specificity HISTONE DEACETYLASE 4, Target Species Human, Host Mouse, Format Azide Free, Isotypes IgG2a, Appli 0.1 mg
MCA4831Z MOUSE ANTI HUMAN HISTONE DEACETYLASE 3 Azide free, Product Type Monoclonal Antibody, Specificity HISTONE DEACETYLASE 3, Target Species Human, Host Mouse, Format Azide Free, Isotypes IgG2a, Appli 0.1 mg
MCA3659Z MOUSE ANTI HUMAN HISTONE DEACETYLASE 6 Azide Free, Product Type Monoclonal Antibody, Specificity HISTONE DEACETYLASE 6, Target Species Human, Host Mouse, Format Azide Free, Isotypes IgG1, Applic 0.1 mg
MCA3883Z MOUSE ANTI HUMAN HISTONE DEACETYLASE 8 Azide Free, Product Type Monoclonal Antibody, Specificity HISTONE DEACETYLASE 8, Target Species Human, Host Mouse, Format Azide Free, Isotypes IgG2b, Appli 0.1 mg
MCA3162Z MOUSE ANTI HUMAN HISTONE DEACETYLASE 1 Azide Free, Product Type Monoclonal Antibody, Specificity HISTONE DEACETYLASE 1, Target Species Human, Host Mouse, Format Azide Free, Isotypes IgG1, Applic 0.1 mg
MCA3587Z MOUSE ANTI HUMAN HISTONE DEACETYLASE 3 Azide Free, Product Type Monoclonal Antibody, Specificity HISTONE DEACETYLASE 3, Target Species Human, Host Mouse, Format Azide Free, Isotypes IgG2a, Appli 0.1 mg
MCA3843Z MOUSE ANTI HUMAN HISTONE DEACETYLASE 7 Azide Free, Product Type Monoclonal Antibody, Specificity HISTONE DEACETYLASE 7, Target Species Human, Host Mouse, Format Azide Free, Isotypes IgG2b, Appli 0.1 mg
MCA3933Z MOUSE ANTI HUMAN HISTONE DEACETYLASE 11 Azide Free, Product Type Monoclonal Antibody, Specificity HISTONE DEACETYLASE 11, Target Species Human, Host Mouse, Format Azide Free, Isotypes IgG1, Appl 0.1 mg
orb61320 CI-994 CI-994 is a histone deacetylase (HDAC) inhibitor and induces histone hyperacetylation in living cells. CI-994 inhibited HDAC-1 and HDAC-2 but not the prototypical histone acetyltransferase GCN5 500 mg
26-515 SPOP may modulate the transcriptional repression activities of death-associated protein 6 (DAXX), which interacts with histone deacetylase, core histones, and other histone-associated proteins. In mou 0.05 mg
28-996 SAP30BP is a component of a histone deacetylase complex conserved among eukaryotic organisms. This complex is active in deacetylating core histone octamers, but inactive in deacetylating nucleosomal h 0.1 mg
28-051 SAP30BP is a component of a histone deacetylase complex conserved among eukaryotic organisms. This complex is active in deacetylating core histone octamers, but inactive in deacetylating nucleosomal h 0.05 mg
49-395 Histone Deacetylase 1 Antibody 0.05 mg
E02H0234 Rat Histone Deacetylase 96 Tests/kit
48-490 Histone Deacetylase 2 Antibody 0.05 mg
48-700 Histone Deacetylase 2 Antibody 0.05 mg
48-701 Histone Deacetylase 4 Antibody 0.05 mg
49-282 Histone Deacetylase 4 Antibody 0.05 mg


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur